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GOT IFCC without Pyridoxalphosphat Fluid 5+1

GOT IFCC without Pyridoxalphosphat Fluid 5+1

Aspartate aminotransferase (glutamate oxaloacetate transaminase) belongs to the transaminases, which catalyze the interconversion of amino acids and a-ketoacids by transfer of amino groups. Aspartate aminotransferase is commonly found in human tissue. Although heart muscle is found to have the most activity of the enzyme, significant activity has also been seen in the brain, liver, gastric mucosa, adipose tissue, skeletal muscle, and kidneys.

AST is present in both the cytoplasm and mitochondria of cells. In cases involving mild tissue injury, the predominant form of AST is that from the cytoplasm, with a smaller amount coming from the mitochondria. Severe tissue damage results in more of the mitochondrial enzyme being released. Elevated levels of the transaminases can signal myocardial infarction, hepatic disease, muscular dystrophy, and organ damage.

In 1955, Karmen et al described the first kinetic determination of AST activity in serum. The International Federation of Clinical Chemistry (IFCC) recommended in 1977 and 1980 standardized procedures for AST determination, including optimization of substrate concentrations, employment of TRIS* buffers, preincubation of combined buffer and serum to allow side reactions with NADH to occur, substrate start, and optional pyridoxal phosphate activation.

This method is derived from the IFCC reterence method.

*TRIS = Tris(hydroxymethyl)-aminomethane

Intended use

In vitro test for the quantitative determination of aspartate amino-transferase (AST) in human serum and plasma

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